Open AccessStructure of d ‐lactate dehydrogenase from Aquifex aeolicus complexed with NAD + and lactic acid (or pyruvate)
Author(s) -
Antonyuk Svetlana V.,
Strange Richard W.,
Ellis Mark J.,
Bessho Yoshitaka,
Kuramitsu Seiki,
Inoue Yumiko,
Yokoyama Shigeyuki,
Hasnain S. Samar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109044935
Subject(s) - aquifex aeolicus , cofactor , pyruvate dehydrogenase kinase , chemistry , nad+ kinase , lactate dehydrogenase , pyruvate dehydrogenase complex , ternary complex , dehydrogenase , stereochemistry , oxidoreductase , crystallography , biochemistry , enzyme , escherichia coli , gene
The crystal structure of d ‐lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 Å resolution in space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 90.94, b = 94.43, c = 188.85 Å. The structure was solved by molecular replacement using the coenzyme‐binding domain of Lactobacillus helveticus d ‐lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a `closed' conformation with the NADH cofactor bound to the coenzyme‐binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active‐site cleft.